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Related to mutase: enolase


 (myo͞o′tās, -tāz)
An enzyme that catalyzes the shifting of a chemical group from one position to another within the same molecule.

[Latin mūtāre, to change, move; see mutate + -ase.]


(Biochemistry) biochem an enzyme which catalyzes the transfer of a functional group between two positions within the same molecule
References in periodicals archive ?
The data, published online in the journal Cell Reports, demonstrate that intravenous administration of an mRNA therapeutic encoding for human methylmalonyl-CoA mutase, the enzyme most frequently mutated in MMA, enabled liver expression of MUT in MMA mouse models, leading to a significant reduction in methylmalonic acid, a substantial improvement in weight gain, and the complete survival of the full cohort of treated mice versus control group.
pylori strain was performed by using specific primers targeting 16S rRNA and ureC encodes for phosphoglucosamine mutase genes.
The target enzyme, cofactor-independent phosphoglycerate mutase (iPGM), is found in both parasites and bacteria.
MMA is caused by a defect in the conversion of L-methylmalonyl-CoA to succinyl-CoA, catalyzed by the enzyme methylmalonylCoA (MMCoA) mutase (EC.
Results have shown a reasonable increase in activity of antioxidant enzyme superoxide dis mutase under different salinity levels.
This organic acid buildup is caused by one of three mechanisms: genetic defect or absence of the enzyme methylmalonic acid coenzyme A mutase (mut), defect in the synthesis and transport of mut's cofactor 5'-deoxyadenosylcobalamin, and defect in the mitochondrial transport of cobalamin.
The glycolysis genes include phosphoglycerate mutase 1 (5223), glyceraldehyde-3-phosphate dehydrogenase (2597), and glucose-6-phosphatase (57818).
Among different Cbl species, only MeCbl and AdoCbl are metabolically active, functioning as cofactors for the cytoplasmic enzyme MS and the mitochondrial enzyme methylmalonyl-CoA mutase, respectively.
Total parenteral nutrition via a central venous catheter Lai 2010 Congenital short bowel Syndrome, hypogammaglobulinemia, Porth-A-cath for total parenteral nutrition Becker 2008 Methylmalonic aciduria due to a noncobalamin- responsive deficiency of methylmalonyl coenzyme A mutase.
Molecular modeling, dynamics, and an insight into the structural inhibition of cofactor independent phosphoglycerate mutase isoform-1 from Wuchereria bancrofti using cheminformatics and mutational studies.
These genes include both the myosin heavy and light chain, and the phosphoglycerate mutase 2 (pgam2) gene.
MMA is a compound that can build up in the bloodstream if there isn't enough vitamin B12 in the body for an enzyme, methylmalonyl-CoA mutase, to function properly.